Structure of PDB 3ut0 Chain A

Receptor sequence
>3ut0A (length=804) Species: 368972 (Pseudoalteromonas sp. BB1) [Search protein sequence]
QVNWPYVNTKLKRDPAVEAQIEKLLAKMTIEQKVAQMIQPEIGYLTVEQM
RKYGFGSYLNGGNTAPYGNKRADQATWLKYADEMYLAAMDSTLDGIAIPT
VWGTDAMHGHSNVYGATLFPHNIGLGAARDTDLIKRIGQATAKEVAATGI
EWSFAPTVAVVRDDRWGRTYESYSEDPDLVKRYAGEMVTGIQGDVGADFL
KGSNRIATAKHFVGDGGTERGVDRGNTLIDEKGLRDIHSAGYFSAINQGV
QSVMASFNSWNGKRVHGDKHLLTDVLKNQLGFDGFVVSDWNAHKFVEGCD
LEQCAQAINAGVDVIMVPEHFEAFYHNTVKQVKAGVIAESRINDAVRRFL
RAKIRWGVFTKSKPSARPESQHPQWLGAAEHRTLAREAVRKSLVLLKNNE
SILPIKASSRILVAGKGANAINMQAGGWSVSWQGTDNTNSDFPNATSIFS
GLQSQVTKAGGKITLSESGEYTSKPDVAIVVIGEEPYAEWFGDIELLEFQ
HETKHALALLKQLKADNIPVVTVFLSGRPLWVNKELNASDAFVAAWLPGS
EGEGVADVLLTNKQGKTQFDFTGKLSFSWPKYDDQFTLNLNDADYDPLFA
YGYGLTYQDNINVPVLSEKTSPSDSHPLFVRSLAKNMTWQLADTSTQKVL
ASGASATSGDKQSLLMQSVNLSYQEDGRGFNWRAQAALSLSYLEPTPLDS
KFSTGYLELKMRIDKAPEQGANLQVMCSESNCLRDIDFSSFSQLMADKSW
HTLAIPLHCDDSEQPITDALRITSQNLSLAIADVALTIKPSDDSISLTCA
KLEH
3D structure
PDB3ut0 Structure and activity of exo-1,3/1,4-beta-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D293 E493
Catalytic site (residue number reindexed from 1) D289 E489
Enzyme Commision number 3.2.1.21: beta-glucosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A E179 L592 N593 E175 L588 N589
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009251 glucan catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3ut0, PDBe:3ut0, PDBj:3ut0
PDBsum3ut0
PubMed22129429
UniProtQ0QJA3

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